Research workbench
Crystal structure of putrescine transcarbamylase from enterococcus faecalis
Analyse Crystal structure of putrescine transcarbamylase from enterococcus faecalis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TXX
- Type
- protein
- Length
- 4,092 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putrescine carbamoyltransferase
- EC
- 2.1.3.6
- UniProt
- Q837U7
- Ligands
- SO4
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 8 distinct chains · 45% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putrescine carbamoyltransferase (EC 2.1.3.6) | protein | 337 | 46% helix, 13% strand | Q837U7 |
| B | Putrescine carbamoyltransferase (EC 2.1.3.6) | protein | 353 | 44% helix, 13% strand | Q837U7 |
| C, F | Putrescine carbamoyltransferase (EC 2.1.3.6) | protein | 340 | 45% helix, 13% strand | Q837U7 |
| D | Putrescine carbamoyltransferase (EC 2.1.3.6) | protein | 347 | 44% helix, 12% strand | Q837U7 |
| E | Putrescine carbamoyltransferase (EC 2.1.3.6) | protein | 343 | 45% helix, 12% strand | Q837U7 |
| G, J, K, L | Putrescine carbamoyltransferase (EC 2.1.3.6) | protein | 341 | 45% helix, 12% strand | Q837U7 |
| H | Putrescine carbamoyltransferase (EC 2.1.3.6) | protein | 336 | 46% helix, 13% strand | Q837U7 |
| I | Putrescine carbamoyltransferase (EC 2.1.3.6) | protein | 332 | 45% helix, 13% strand | Q837U7 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 27 copies · chains A, B, C, E, D, F, G, H, I, J, L, K
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 877 | 0.81 | 0.83 | 130 | SO4 |
| 2 | 957 | 0.73 | 0.77 | 85 | empty |
| 3 | 573 | 0.73 | 0.81 | 69 | SO4 |
| 4 | 541 | 0.70 | 0.79 | 60 | SO4 |
| 5 | 558 | 0.69 | 0.78 | 53 | SO4 |
Interfaces
20 interfaces between chains.
- D–F · 1914 Ų buried · 32 hydrogen bonds · protein-protein
- J–L · 1853 Ų buried · 22 hydrogen bonds · protein-protein
- B–C · 1827 Ų buried · 26 hydrogen bonds · protein-protein
- G–I · 1824 Ų buried · 29 hydrogen bonds · protein-protein
- D–E · 1812 Ų buried · 27 hydrogen bonds · protein-protein
Compared structures
- 3TXX · Crystal structure of putrescine transcarbamylase from Enterococcus faecalis · the same entry in another collection · chain L against L, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q837U7
- Elsewhere: RCSB PDB 3TXX · PDBe 3TXX · UniProt Q837U7
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